title: New insights into the mechanism of force generation by kinesin-5 molecular motors.
abstract: Kinesin-5 motors are members of a superfamily of microtubule-dependent ATPases and are widely conserved among eukaryotes. Kinesin-5s typically form homotetramers with pairs of motor domains located at either end of a dumbbell-shaped molecule. This quaternary structure enables cross-linking and ATP-driven sliding of pairs of microtubules, although the exact molecular mechanism of this activity is still unclear. Kinesin-5 function has been characterized in greatest detail in cell division, although a number of interphase roles have also been defined. The kinesin-5 ATPase is tuned for slow microtubule sliding rather than cellular transport and-in vertebrates-can be inhibited specifically by allosteric small molecules currently in cancer clinical trials. The biophysical and structural basis of kinesin-5 mechanochemistry is being elucidated and has provided further insight into kinesin-5 activities. However, it is likely that the precise mechanism of these important motors has evolved according to functional context and regulation in individual organisms.
authors.affiliation: Institute of Structural and Molecular Biology, Birkbeck College, London, United Kingdom.
authors.forename: Adeline
authors.initials: A
authors.lastname: Goulet
authors.forename: Carolyn
authors.initials: C
authors.lastname: Moores
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D002465:Cell Movement; D002477:Cells / Q000166:cytology / Q000378:metabolism; D006801:Humans; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological
chemical_list: D016547:Kinesins